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P04896

- GNAS2_BOVIN

UniProt

P04896 - GNAS2_BOVIN

Protein

Guanine nucleotide-binding protein G(s) subunit alpha isoforms short

Gene

GNAS

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase: it activates the cyclase in response to beta-adrenergic stimuli. Stimulates the Ras signaling pathway via RAPGEF2 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi54 – 541MagnesiumBy similarity
    Metal bindingi204 – 2041MagnesiumBy similarity
    Binding sitei366 – 3661GTP; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi47 – 548GTPBy similarity
    Nucleotide bindingi198 – 2047GTPBy similarity
    Nucleotide bindingi223 – 2275GTPBy similarity
    Nucleotide bindingi292 – 2954GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: InterPro
    2. GTP binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. signal transducer activity Source: UniProtKB

    GO - Biological processi

    1. adenylate cyclase-activating adrenergic receptor signaling pathway Source: UniProtKB
    2. adenylate cyclase-activating dopamine receptor signaling pathway Source: Ensembl
    3. cartilage development Source: Ensembl
    4. DNA methylation Source: Ensembl
    5. embryonic cranial skeleton morphogenesis Source: Ensembl
    6. embryonic hindlimb morphogenesis Source: Ensembl
    7. endochondral ossification Source: Ensembl
    8. energy reserve metabolic process Source: Ensembl
    9. genetic imprinting Source: Ensembl
    10. multicellular organism growth Source: Ensembl
    11. positive regulation of cAMP biosynthetic process Source: UniProtKB
    12. positive regulation of cAMP-mediated signaling Source: UniProtKB
    13. positive regulation of osteoblast differentiation Source: Ensembl
    14. positive regulation of osteoclast differentiation Source: Ensembl
    15. positive regulation of Ras GTPase activity Source: UniProtKB
    16. post-embryonic body morphogenesis Source: Ensembl
    17. response to drug Source: Ensembl
    18. skin development Source: Ensembl
    19. tissue homeostasis Source: Ensembl

    Keywords - Molecular functioni

    Transducer

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_202137. Regulation of water balance by renal Aquaporins.
    REACT_206547. G alpha (s) signalling events.
    REACT_209033. G alpha (z) signalling events.
    REACT_210568. G alpha (i) signalling events.
    REACT_217846. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_219718. PKA activation in glucagon signalling.
    REACT_220607. Glucagon-type ligand receptors.
    REACT_221707. Glucagon signaling in metabolic regulation.
    REACT_227415. Prostacyclin signalling through prostacyclin receptor.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
    Alternative name(s):
    Adenylate cyclase-stimulating G alpha protein
    Gene namesi
    Name:GNAS
    Synonyms:GNAS1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    Cell membrane By similarity; Lipid-anchor By similarity

    GO - Cellular componenti

    1. dendrite Source: Ensembl
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 394394Guanine nucleotide-binding protein G(s) subunit alpha isoforms shortPRO_0000203717Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-palmitoyl glycine1 Publication
    Lipidationi3 – 31S-palmitoyl cysteine1 Publication
    Cross-linki300 – 300Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei352 – 3521PhosphoserineBy similarity

    Keywords - PTMi

    Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP04896.

    Interactioni

    Subunit structurei

    G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with CRY1; the interaction may block GPCR-mediated regulation of cAMP concentrations.

    Protein-protein interaction databases

    DIPiDIP-588N.
    IntActiP04896. 1 interaction.
    STRINGi9913.ENSBTAP00000023234.

    Structurei

    Secondary structure

    1
    394
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi36 – 394
    Beta strandi40 – 489
    Helixi53 – 6412
    Helixi87 – 893
    Helixi90 – 11223
    Beta strandi113 – 1153
    Helixi122 – 1243
    Helixi125 – 1339
    Turni134 – 1363
    Helixi144 – 15512
    Helixi157 – 1637
    Helixi164 – 1685
    Helixi175 – 1795
    Helixi182 – 1854
    Beta strandi187 – 1893
    Helixi194 – 1996
    Beta strandi206 – 2149
    Beta strandi217 – 2248
    Helixi228 – 23710
    Turni238 – 2403
    Beta strandi243 – 2497
    Helixi252 – 2543
    Turni258 – 2603
    Beta strandi261 – 2644
    Helixi265 – 27713
    Helixi280 – 2823
    Beta strandi283 – 2853
    Beta strandi287 – 2926
    Helixi294 – 30310
    Helixi308 – 3103
    Helixi313 – 3164
    Helixi332 – 35019
    Turni354 – 3563
    Beta strandi359 – 3635
    Beta strandi365 – 3673
    Helixi369 – 39224

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AZSX-ray2.30C1-394[»]
    1AZTX-ray2.30A/B1-394[»]
    1CJKX-ray3.00C1-394[»]
    1CJTX-ray2.80C1-394[»]
    1CJUX-ray2.80C1-394[»]
    1CJVX-ray3.00C1-394[»]
    1CS4X-ray2.50C1-394[»]
    1CULX-ray2.40C1-394[»]
    1TL7X-ray2.80C1-394[»]
    1U0HX-ray2.90C1-394[»]
    2GVDX-ray2.90C1-394[»]
    2GVZX-ray3.27C1-394[»]
    3C14X-ray2.68C1-394[»]
    3C15X-ray2.78C1-394[»]
    3C16X-ray2.87C1-394[»]
    3G82X-ray3.11C1-394[»]
    3MAAX-ray3.00C1-394[»]
    3SN6X-ray3.20A1-394[»]
    ProteinModelPortaliP04896.
    SMRiP04896. Positions 35-391.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04896.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the G-alpha family. G(s) subfamily.Curated

    Phylogenomic databases

    eggNOGiNOG325092.
    HOGENOMiHOG000038729.
    HOVERGENiHBG063184.
    KOiK04632.

    Family and domain databases

    Gene3Di1.10.400.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR000367. Gprotein_alpha_S.
    IPR001019. Gprotein_alpha_su.
    IPR011025. GproteinA_insert.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR10218. PTHR10218. 1 hit.
    PfamiPF00503. G-alpha. 1 hit.
    [Graphical view]
    PRINTSiPR00318. GPROTEINA.
    PR00443. GPROTEINAS.
    SMARTiSM00275. G_alpha. 1 hit.
    [Graphical view]
    SUPFAMiSSF47895. SSF47895. 1 hit.
    SSF52540. SSF52540. 2 hits.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Gnas-1 (identifier: P04896-1) [UniParc]FASTAAdd to Basket

    Also known as: Alpha-S2

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGCLGNSKTE DQRNEEKAQR EANKKIEKQL QKDKQVYRAT HRLLLLGAGE    50
    SGKSTIVKQM RILHVNGFNG EGGEEDPQAA RSNSDGEKAT KVQDIKNNLK 100
    EAIETIVAAM SNLVPPVELA NPENQFRVDY ILSVMNVPDF DFPPEFYEHA 150
    KALWEDEGVR ACYERSNEYQ LIDCAQYFLD KIDVIKQDDY VPSDQDLLRC 200
    RVLTSGIFET KFQVDKVNFH MFDVGGQRDE RRKWIQCFND VTAIIFVVAS 250
    SSYNMVIRED NQTNRLQEAL NLFKSIWNNR WLRTISVILF LNKQDLLAEK 300
    VLAGKSKIED YFPEFARYTT PEDATPEPGE DPRVTRAKYF IRDEFLRIST 350
    ASGDGRHYCY PHFTCAVDTE NIRRVFNDCR DIIQRMHLRQ YELL 394
    Length:394
    Mass (Da):45,709
    Last modified:August 13, 1987 - v1
    Checksum:i4D07A734AFF2A6BC
    GO
    Isoform Gnas-2 (identifier: P04896-2) [UniParc]FASTAAdd to Basket

    Also known as: Alpha-S1

    The sequence of this isoform differs from the canonical sequence as follows:
         71-84: Missing.

    Show »
    Length:380
    Mass (Da):44,280
    Checksum:i5B06C75B1A366920
    GO
    Isoform Nesp55 (identifier: O18979-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry O18979.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Shares no sequence similarity with other isoforms due to a novel first exon containing the entire reading frame spliced to shared exon 2 so that exons 2-13 make up the 3'-UTR.

    Length:241
    Mass (Da):27,494
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181A → G in AAA30560. (PubMed:3081893)Curated
    Sequence conflicti85 – 851D → S in AAA30560. (PubMed:3081893)Curated
    Sequence conflicti363 – 3631F → S in AAA30560. (PubMed:3081893)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei71 – 8414Missing in isoform Gnas-2. CuratedVSP_001832Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03404 mRNA. Translation: CAA27137.1.
    M13006 mRNA. Translation: AAA30560.1.
    BC102905 mRNA. Translation: AAI02906.1.
    BC122757 mRNA. Translation: AAI22758.1.
    M14014 mRNA. Translation: AAA30557.1.
    PIRiA23818. RGBOGA.
    I45904.
    RefSeqiNP_001258700.1. NM_001271771.1.
    NP_851364.1. NM_181021.3. [P04896-1]
    UniGeneiBt.64619.
    Bt.91987.

    Genome annotation databases

    GeneIDi281793.
    KEGGibta:281793.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03404 mRNA. Translation: CAA27137.1 .
    M13006 mRNA. Translation: AAA30560.1 .
    BC102905 mRNA. Translation: AAI02906.1 .
    BC122757 mRNA. Translation: AAI22758.1 .
    M14014 mRNA. Translation: AAA30557.1 .
    PIRi A23818. RGBOGA.
    I45904.
    RefSeqi NP_001258700.1. NM_001271771.1.
    NP_851364.1. NM_181021.3. [P04896-1 ]
    UniGenei Bt.64619.
    Bt.91987.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AZS X-ray 2.30 C 1-394 [» ]
    1AZT X-ray 2.30 A/B 1-394 [» ]
    1CJK X-ray 3.00 C 1-394 [» ]
    1CJT X-ray 2.80 C 1-394 [» ]
    1CJU X-ray 2.80 C 1-394 [» ]
    1CJV X-ray 3.00 C 1-394 [» ]
    1CS4 X-ray 2.50 C 1-394 [» ]
    1CUL X-ray 2.40 C 1-394 [» ]
    1TL7 X-ray 2.80 C 1-394 [» ]
    1U0H X-ray 2.90 C 1-394 [» ]
    2GVD X-ray 2.90 C 1-394 [» ]
    2GVZ X-ray 3.27 C 1-394 [» ]
    3C14 X-ray 2.68 C 1-394 [» ]
    3C15 X-ray 2.78 C 1-394 [» ]
    3C16 X-ray 2.87 C 1-394 [» ]
    3G82 X-ray 3.11 C 1-394 [» ]
    3MAA X-ray 3.00 C 1-394 [» ]
    3SN6 X-ray 3.20 A 1-394 [» ]
    ProteinModelPortali P04896.
    SMRi P04896. Positions 35-391.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-588N.
    IntActi P04896. 1 interaction.
    STRINGi 9913.ENSBTAP00000023234.

    Proteomic databases

    PRIDEi P04896.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 281793.
    KEGGi bta:281793.

    Organism-specific databases

    CTDi 2778.

    Phylogenomic databases

    eggNOGi NOG325092.
    HOGENOMi HOG000038729.
    HOVERGENi HBG063184.
    KOi K04632.

    Enzyme and pathway databases

    Reactomei REACT_202137. Regulation of water balance by renal Aquaporins.
    REACT_206547. G alpha (s) signalling events.
    REACT_209033. G alpha (z) signalling events.
    REACT_210568. G alpha (i) signalling events.
    REACT_217846. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_219718. PKA activation in glucagon signalling.
    REACT_220607. Glucagon-type ligand receptors.
    REACT_221707. Glucagon signaling in metabolic regulation.
    REACT_227415. Prostacyclin signalling through prostacyclin receptor.

    Miscellaneous databases

    EvolutionaryTracei P04896.
    NextBioi 20805706.

    Family and domain databases

    Gene3Di 1.10.400.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR000367. Gprotein_alpha_S.
    IPR001019. Gprotein_alpha_su.
    IPR011025. GproteinA_insert.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR10218. PTHR10218. 1 hit.
    Pfami PF00503. G-alpha. 1 hit.
    [Graphical view ]
    PRINTSi PR00318. GPROTEINA.
    PR00443. GPROTEINAS.
    SMARTi SM00275. G_alpha. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47895. SSF47895. 1 hit.
    SSF52540. SSF52540. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the alpha-subunit of bovine adenylate cyclase-stimulating G-protein deduced from the cDNA sequence."
      Nukada T., Tanabe T., Takahashi H., Noda M., Hirose T., Inayama S., Numa S.
      FEBS Lett. 195:220-224(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Deduced primary structure of the alpha subunit of the GTP-binding stimulatory protein of adenylate cyclase."
      Robishaw J.D., Russell D.W., Harris B.A., Smigel M.D., Gilman A.G.
      Proc. Natl. Acad. Sci. U.S.A. 83:1251-1255(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Hypothalamus and Kidney.
    4. "Molecular basis for two forms of the G protein that stimulates adenylate cyclase."
      Robishaw J.D., Smigel M.D., Gilman A.G.
      J. Biol. Chem. 261:9587-9590(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-90.
    5. "Galpha(s) is palmitoylated at the N-terminal glycine."
      Kleuss C., Krause E.
      EMBO J. 22:826-832(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT GLY-2 AND CYS-3, IDENTIFICATION BY MASS SPECTROMETRY.
    6. "Crystal structure of the adenylyl cyclase activator Gsalpha."
      Sunahara R.K., Tesmer J.J.G., Gilman A.G., Sprang S.R.
      Science 278:1943-1947(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-394 OF GNAS-2 FORM.
    7. "Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS."
      Tesmer J.J.G., Sunahara R.K., Gilman A.G., Sprang S.R.
      Science 278:1907-1916(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH CATALYTIC DOMAINS OF ADENYLATE CYCLASE.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH CATALYTIC DOMAINS OF ADENYLATE CYCLASE.

    Entry informationi

    Entry nameiGNAS2_BOVIN
    AccessioniPrimary (citable) accession number: P04896
    Secondary accession number(s): Q0II85, Q3SZE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 151 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The GNAS locus is imprinted in a complex manner, giving rise to distinct paternally, maternally and biallelically expressed proteins.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3